Safe, live Vibrio cholerae vaccines?

Taylor, Ronald K.; Shaw, Carolyn E.; Peterson, Kenneth M.; Spears, Patricia A.; Mekalanos, John J.

doi:10.1016/s0264-410x(88)80019-7

Cited by 109 publications

(67 citation statements)

References 5 publications

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“…Amino-terminal sequence and modification of TcpA. The first 32 residues of 23-kD TcpA correspond to those predicted by DNA sequence analysis and overlap previously determined residues from mature pilin (Taylor et al 1988). The site of proteolytic cleavage of prepilin is indicated by a vertical arrow.…”

Section: Nucleotide Sequence Of Tcpj and Properties Of The Deduced Prsupporting

confidence: 54%

“…Two classes of cosmid clones were identified: those that expressed TcpA in the expected 20.5-kD form, and those that synthesized a 23-kD cross-reactive protein thought to be a pilin precursor, suggesting the presence of linked genes encoding products required for TcpA maturation (Shaw and Taylor 1990). Deletion mapping and TnphoA mutagenesis of these cosmids determined that secretion of the TCP pilin subunit and organelle biogenesis require the products of at least seven genes located adjacent to tcpA {Taylor et al 1988). The region downstream of tcpA necessary for conversion of pilin to its mature 20.5-kD form was localized to a 3.3-kb HindIII-EcoRV restriction fragment present on pCS19H (Shaw 1988).…”

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confidence: 99%

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Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Kaufman¹,

Seyer²,

Taylor³

1991

Genes Dev.

103

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Biogenesis of the Vibrio cholerae toxin-coregulated pilus (TCP) requires the activities of at least seven accessory proteins. We demonstrate that a portion of this pathway involves a novel processing step in which a hydrophilic leader peptide is proteolytically removed from TcpA by the gene product characterized in this report, TcpJ, to yield the mature, export-competent form of the pilin. Cleavage of the pilin leader peptide is independent of known signal peptidases as demonstrated by pilin-processing profiles in Escherichia coli strains conditionally defective for production of leader peptidase or grown in the presence of the antibiotic globomycin. Additionally, pilin cleavage did not rely on the SecA protein, as evidenced by TcpA processing in azide-treated cells. These results suggest that TcpJ is representative of a new class of proteins involved in SecA-independent proteolytic cleavage of a set of atypical leader peptides during extracellular export.

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Section: Nucleotide Sequence Of Tcpj and Properties Of The Deduced Prsupporting

confidence: 54%

mentioning

confidence: 99%

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Kaufman¹,

Seyer²,

Taylor³

1991

Genes Dev.

103

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“…TcpP and TcpH have been shown to regulate CT and TCP expression possibly through ToxT (Carroll et al, 1997;Häse & Mekalanos, 1998). The majority of V. cholerae serotypes do not contain genes for CT and TCP (Taylor et al, 1988;Bakhshi et al, 2009), whereas the gene for ToxR is ubiquitously present (Nandi et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Characterization of pathogenicity island prophage in clinical and environmental strains of Vibrio cholerae

Mohammadi-Barzelighi

Bakhshi

Lari

et al. 2011

Journal of Medical Microbiology

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In this study 86 isolates of Vibrio cholerae were analysed for their adhesive properties and the presence of pathogenicity island genes. With the exception of three isolates, all of the other clinical isolates (92.5 %) contained an intact TCP (toxin-co-regulated pilus) gene cluster. In contrast, 95 % of all environmental non-O1-non-O139 isolates were negative for the TCP gene cluster. The majority of clinical isolates (82.5 %) possessed the complete vibrio pathogenicity island (VPI) gene cluster and had a similar RFLP pattern, while only a single environmental strain possessed an almost complete VPI cluster (lacking 0.4 kb in the tcpA and toxT region). The result showed that the isolates with tcpA + /toxT + had a strong attachment for HT-29 and Vero cells, whereas isolates with tcpA + /toxT " or tcpA " /toxT " genomic characteristics showed no autoagglutination and weak attachment for the cell lines. Two environmental strains (tcpA " /toxT " ) showed strong adhesive properties to the cell lines, indicating that non-fimbrial adhesive factors are involved in the environmental V. cholerae strains in the absence of TCP.

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“…Under ToxR-inducing environmental conditions, there is enhanced expression of toxT at the ToxR-dependent promoter, activation of the tcpA promoter by ToxT and positive autoregulation of toxT in a transcript originating at the upstream tcpA promoter (Brown and Taylor, 1995). Taylor et al (1988) have previously used TnphoA mutagenesis to identify genes in V. cholerae that are ToxR regulated and affect autoagglutination (a phenotype correlated with production of Tcp). In addition to genes in the tcpA operon, these studies disclosed two genes upstream of tcpA, tcpH (transcribed in the same direction as tcpA) and tcpI (divergently transcribed); the phenotypes of mutations in these genes suggested that TcpH was a positive regulator of the tcpA operon and TcpI was a negative regulator.…”

Section: Introductionmentioning

confidence: 99%

Phase variation in tcpH modulates expression of the ToxR regulon in Vibrio cholerae

Carroll

Tashima

Rogers

et al. 1997

Molecular Microbiology

123

126

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SummaryWe evaluated a spontaneous mutant of Vibrio cholerae, which was avirulent in an infant mouse and had reduced expression of cholera toxin and TcpA in response to environmental signals. The toxR, toxS and toxT genes in the mutant were normal, but transcription of toxT was absent. A plasmid expressing wild-type tcpP and tcpH complemented the mutant. The mutation resulted from a frameshift in a string of nine G residues within tcpH; similar slipped-strand mutations in tcpH arose at a frequency of 10 ¹4 during overnight growth and in the majority of colonies by the end of 5 days of growth in ToxR-inducing conditions. Transcription of tcpPH was regulated by temperature and pH independently of ToxR or ToxT. These results suggest that TcpH couples environmental signals (temperature and pH) to expression of the ToxR regulon, and provide a model for phase variation in the co-ordinate expression of cholera virulence factors.

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Safe, live Vibrio cholerae vaccines?

Cited by 109 publications

References 5 publications

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Characterization of pathogenicity island prophage in clinical and environmental strains of Vibrio cholerae

Phase variation in tcpH modulates expression of the ToxR regulon in Vibrio cholerae

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